Journal
EMBO JOURNAL
Volume 40, Issue 6, Pages -Publisher
WILEY
DOI: 10.15252/embj.2020106449
Keywords
ABC ATPase; cryo‐ EM; eEF3; E‐ site tRNA; L1 stalk
Categories
Funding
- iNEXT [2643]
- Horizon 2020 program of the European Union (CEITEC MU)
- NIH [R37GM059425]
- HHMI
- Deutsche Forschungsgemeinschaft (DFG) [WI3285/8-1, RA 3194/1-1]
- MEYS CR [LM2015043]
- ProjektDEAL
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Research suggests that eEF3 functions in the mRNA-tRNA translocation process, aiding in the release of E-site tRNA and speeding up translocation by promoting non-rotated ribosomal states. Depletion of eEF3 results in a general slowdown of translation elongation, providing new structural insights into the yeast translation elongation cycle.
In addition to the conserved translation elongation factors eEF1A and eEF2, fungi require a third essential elongation factor, eEF3. While eEF3 has been implicated in tRNA binding and release at the ribosomal A and E sites, its exact mechanism of action is unclear. Here, we show that eEF3 acts at the mRNA-tRNA translocation step by promoting the dissociation of the tRNA from the E site, but independent of aminoacyl-tRNA recruitment to the A site. Depletion of eEF3 in vivo leads to a general slowdown in translation elongation due to accumulation of ribosomes with an occupied A site. Cryo-EM analysis of native eEF3-ribosome complexes shows that eEF3 facilitates late steps of translocation by favoring non-rotated ribosomal states, as well as by opening the L1 stalk to release the E-site tRNA. Additionally, our analysis provides structural insights into novel translation elongation states, enabling presentation of a revised yeast translation elongation cycle.
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